IF4G1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IF4G1_ARATH
• UniProt AC: Q93ZT6
• Protein Name: Eukaryotic translation initiation factor isoform 4G-1
• Gene Name: EIF(ISO)4G1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 780
• Protein Description: Plays a role in the accumulation of some potyvirus during viral infection..
• Protein Sequence: MQQGDQTVLSLRPGGGRGNRLFGSSSSSSSLSFGSLSSSDLPLLRPHGGAPASSFPFKGGDSRFDGRERVKYTREQLLELKETTQLSDEILRVQRETAAELFGEEGTWARGESVVSNLVPVQSASRFSEPDSRDWRSRSTQPPPSGEERSWDNLREAKDSRYVEASQYNRQDQPNSQFSRANISSNQGGGPAPVLVKAEVPWSARRGNLSENDRVLKTVKGILNKLTPEKYDLLKGQLIESGITSADILKGVITLIFDKAVLEPTFCPMYAKLCSDINDQLPTFPPAEPGDKEITFKRVLLNICQEAFEGASQLREELRQMSAPDQEAERNDKEKLLKLKTLGNIRLIGELLKQKMVPEKIVHHIVQELLGADEKVCPAEENVEAICHFFKTIGKQLDGNVKSKRINDVYFKRLQALSKNPQLELRLRFMVQNIIDMRSNGWVPRREEMKARTITEIHTEAEKNLGLRPGATANMRRGMVSSGGPVSPGPVYPGGRPGAGGLMPGMPGTRRMPGMPGVDNDNWEVPRTRSMSRRDGPGPLHSPAVSKSASMNTRLLPQGSSGIMSGKTSALLQGSGSVSRPVTVSAERPAQSVAPLTVPVPVEKPQPSGPKLSEEVLQRKTKSLLEEYFNVRLLGEALQCVEELGLPSYHPEFVKEAISLSLEKSPPVVEPIATLLEYLLSKKVVAPKDLETGFLLYGAMLDDIGIDLPKAPNNFGEIVGKLILAGGVDFKLVREIIGKMEDDRFQKMVVDAAVRIVESSEQGKSLLASQAADIEACRNL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
116	Phosphorylation	ARGESVVSNLVPVQS CCCCCHHHHCEECCC	39.77	25561503
123	Phosphorylation	SNLVPVQSASRFSEP HHCEECCCCCCCCCC	50.95	30407730
125	Phosphorylation	LVPVQSASRFSEPDS CEECCCCCCCCCCCC	22.99	30407730
137	Phosphorylation	PDSRDWRSRSTQPPP CCCCCHHHCCCCCCC	4.19	25561503
139	Phosphorylation	SRDWRSRSTQPPPSG CCCHHHCCCCCCCCC	24.92	29654922
140	Phosphorylation	RDWRSRSTQPPPSGE CCHHHCCCCCCCCCC	21.32	25561503
481	Phosphorylation	NMRRGMVSSGGPVSP CCCCCCCCCCCCCCC	30.57	24601666
482	Phosphorylation	MRRGMVSSGGPVSPG CCCCCCCCCCCCCCC	47.24	24601666
487	Phosphorylation	VSSGGPVSPGPVYPG CCCCCCCCCCCCCCC	19.07	23111157
492	Phosphorylation	PVSPGPVYPGGRPGA CCCCCCCCCCCCCCC	5.95	24601666
542	Phosphorylation	DGPGPLHSPAVSKSA CCCCCCCCCCCCCCC	17.52	30589143
546	Phosphorylation	PLHSPAVSKSASMNT CCCCCCCCCCCCCCC	32.11	25561503
548	Phosphorylation	HSPAVSKSASMNTRL CCCCCCCCCCCCCCC	60.63	25368622
550	Phosphorylation	PAVSKSASMNTRLLP CCCCCCCCCCCCCCC	6.77	28011693
553	Phosphorylation	SKSASMNTRLLPQGS CCCCCCCCCCCCCCC	2.38	25368622
560	Phosphorylation	TRLLPQGSSGIMSGK CCCCCCCCCCCCCCC	50.35	25368622
561	Phosphorylation	RLLPQGSSGIMSGKT CCCCCCCCCCCCCCC	42.77	25368622
565	Phosphorylation	QGSSGIMSGKTSALL CCCCCCCCCCCCHHH	7.41	25368622
575	Phosphorylation	TSALLQGSGSVSRPV CCHHHCCCCCCCCCE	31.18	25561503
577	Phosphorylation	ALLQGSGSVSRPVTV HHHCCCCCCCCCEEE	24.73	25561503
579	Phosphorylation	LQGSGSVSRPVTVSA HCCCCCCCCCEEECC	35.96	25561503
583	Phosphorylation	GSVSRPVTVSAERPA CCCCCCEEECCCCCC	27.88	25561503
585	Phosphorylation	VSRPVTVSAERPAQS CCCCEEECCCCCCCC	33.74	25561503
759	Phosphorylation	AAVRIVESSEQGKSL HHHHHHHCCHHHHHH	39.21	19880383
760	Phosphorylation	AVRIVESSEQGKSLL HHHHHHCCHHHHHHH	3.27	19880383

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of IF4G1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IF4G1_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of IF4G1_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of IF4G1_ARATH !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; THR-178; SER-985 ANDSER-1529, AND MASS SPECTROMETRY.
PubMed: 19376835

"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1529, AND MASSSPECTROMETRY.
PubMed: 19245862